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UniProt release 2012_10

Published October 31, 2012

Headline

CIA: on your Genome service

Life evolved in an anaerobic world and it is thought that iron-sulfur (Fe-S) clusters played a crucial role in this process by facilitating chemical transformations. Once photosynthesis evolved, oxygen became prevalent, threatening Fe-S clusters as they are susceptible to destruction by oxidation. Despite this potential problem, Fe-S clusters are still cofactors in hundreds of proteins. They are required in virtually all organisms from bacteria to humans and are involved not only in ‘redox’ catalysis in some enzymes, but also in many other functions. Interestingly, Fe-S clusters have been found in many proteins involved in DNA repair and replication and telomere length maintenance.

In eukaryotic cells, most biosynthesis of Fe-S clusters occurs in the mitochondria, but it may also occur in the cytosol and nucleus. In the cytosol, Fe-S clusters are escorted and presented to their cytoplasmic and nuclear apoproteins by the conserved cytoplasmic iron-sulfur assembly (CIA) machinery. However, it is not clear how Fe-S clusters are transferred to target apoproteins, nor how target specificity is achieved.

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